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B0KAA6 (SYE2_THEP3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate--tRNA ligase 2

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 2
Short name=GluRS 2
Gene names
Name:gltX2
Ordered Locus Names:Teth39_1419
OrganismThermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium thermohydrosulfuricum) [Complete proteome] [HAMAP]
Taxonomic identifier340099 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeThermoanaerobacter

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) By similarity. HAMAP-Rule MF_00022

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00022

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00022.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 479479Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000367782

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif243 – 2475"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2461ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B0KAA6 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: E50EFBF844346129

FASTA47955,696
        10         20         30         40         50         60 
MSEVRVRFAP SPTGSLHIGG ARTALFNWLF ARHNGGKFIL RVDDTDLQRS TEESMKGILE 

        70         80         90        100        110        120 
GLKWLGIDWD EGPIYQSQRL EEYRKFANKL LKEGKAYYCF CTKEELEEMR KQAEKEGRPP 

       130        140        150        160        170        180 
MYTGKCRNLT KEQIEEYLRQ GKKPVIRLKV PQQGKTVVHD IIRGDVEFDN STFDDFIIMK 

       190        200        210        220        230        240 
SDNMPTYNFA TVVDDYQMGI THVIRAEEHL SNTPKQILIF EALGLEIPQF AHVSMVLAPD 

       250        260        270        280        290        300 
RSKLSKRHGA TSVQEFRDQG YLPEAIVNYI TLLGWIPKDG EEIFDVSKSK KEFTLERVSK 

       310        320        330        340        350        360 
NPAIYDVQKL TWINGHYIRN YDLDKLTEVV IPFLKAKNFI GEDFDYDYIK KIVSVVRERE 

       370        380        390        400        410        420 
KTLVDVADAM SYYFTEVYEY EEKGVKKYFT KEKVVDILKK AVVTLKEVEP FNKFTTEEAY 

       430        440        450        460        470 
RKLVEELQIS SGELFHPTRL AISGRTFGPG LFDIMELLGK ERTIERIEKA IDFIQKMRK 

« Hide

References

[1]"Complete sequence of Thermoanaerobacter pseudethanolicus 39E."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33223 / 39E.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000924 Genomic DNA. Translation: ABY95069.1.
RefSeqYP_001665405.1. NC_010321.1.

3D structure databases

ProteinModelPortalB0KAA6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING340099.Teth39_1419.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY95069; ABY95069; Teth39_1419.
GeneID5874954.
KEGGtpd:Teth39_1419.
PATRIC23887544. VBIThePse6203_1477.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAWINGYYL.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycTPSE340099:GH4W-1459-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
1.10.8.70. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020752. aa-tRNA-synth_I_codon-bd_sub1.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. SSF48163. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE2_THEP3
AccessionPrimary (citable) accession number: B0KAA6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 18, 2008
Last modified: May 14, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries